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International
Tables for Crystallography Volume F Crystallography of biological macromolecules Edited by M. G. Rossmann and E. Arnold © International Union of Crystallography 2006 |
International Tables for Crystallography (2006). Vol. F. ch. 21.2, p. 518
Section 21.2.5. Concluding remarks
aUnité de Conformation de Macromolécules Biologiques, Université Libre de Bruxelles, avenue F. D. Roosevelt 50, CP160/16, B-1050 Bruxelles, Belgium, and EMBL–EBI, Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SD, England, bUnité de Conformation de Macromolécules Biologiques, Université Libre de Bruxelles, avenue F. D. Roosevelt 50, CP160/16, B-1050 Bruxelles, Belgium, and cDepartment of Chemistry, Rutgers University, 610 Taylor Road, Piscataway, NJ 08854-8087, USA |
The coming years will see an ever-increasing number of crystal structures of proteins and nucleic acids determined at high resolution and a substantial growth in the number of atomic resolution structures. This will most certainly help in obtaining better data on the geometric and stereochemical parameters of these macromolecules and thus improve the target values for both refinement and structure validation. It should also make it possible to derive better criteria for evaluating the agreement of the model with the electron density and to improve upon and generalize comprehensive and systematic approaches, such as that implemented in the software SFCHECK.
References
Agarwal, R. C. (1978). A new least-squares refinement technique based on the fast Fourier transform algorithm. Acta Cryst. A34, 791–809.Google Scholar
Cruickshank, D. W. J. (1949). The accuracy of electron-density maps in X-ray analysis with special reference to dibenzyl. Acta Cryst. 2, 65–82.Google Scholar
Cruickshank, D. W. J. (1996). Protein precision re-examined: Luzzati plots do not estimate final errors. In Proceedings of the CCP4 study weekend. Macromolecular refinement, edited by E. Dodson, M. Moore, A. Ralph & S. Bailey, pp. 11–22. Warrington: Daresbury Laboratory.Google Scholar
Das, U., Chen, S., Fuxreiter, M., Vaguine, A. A., Richelle, J., Berman, H. M. & Wodak, S. J. (2001). Checking nucleic acid crystal structures. Acta Cryst. D57, 813–828.Google Scholar
Murshudov, G. N., Vagin, A. A. & Dodson, E. J. (1997). Refinement of macromolecular structures by the maximum-likelihood method. Acta Cryst. D53, 240–255.Google Scholar
Tickle, I. J., Laskowski, R. A. & Moss, D. S. (1998). Error estimates of protein structure coordinates and deviations from standard geometry by full-matrix refinement of γB- and βB2-crystallin. Acta Cryst. D54, 243–252.Google Scholar
Vaguine, A. A., Richelle, J. & Wodak, S. J. (1999). SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model. Acta Cryst. D55, 191–205.Google Scholar
Walter, R. L., Ealick, S. E., Friedman, A. M., Blake, R. C. II, Proctor, P. & Shoham, M. (1996). Multiple wavelength anomalous diffraction (MAD) crystal structure of rusticyanin: a highly oxidizing cupredoxin with extreme acid stability. J. Mol. Biol. 263, 730–749.Google Scholar
